High performance ion exchange chromatography of human plasma lecithin: Cholesterol acyltransferase

1989 ◽  
Vol 3 (6) ◽  
pp. 276-278 ◽  
Author(s):  
Leif Holmquist
Keyword(s):  
Ion Exchange ◽  
Human Plasma ◽  
High Performance ◽  
Cholesterol Acyltransferase ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Lecithin Cholesterol Acyltransferase

scholarly journals Biochemical and Kinetic Study for the partially purified Lecithin: Cholesterol acyltransferase from serum cardiovascular disease

2020 ◽  
Vol 25 (2) ◽  
pp. 31
Author(s):  
Amel Taha Yassein Al-Juraisy1 ◽  
Ameera Aziz Mahmood Al-Juraisy1 ◽  
Ameera Aziz Mahmood Al-Juraisy1 ◽  
Nadia Ahmed Saleh2
Keyword(s):  
Cardiovascular Disease ◽  
Molecular Weight ◽  
Ion Exchange ◽  
Cholesterol Acyltransferase ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Partial Purification ◽  
Lecithin Cholesterol Acyltransferase ◽  
Ammonium Sulphate Precipitation ◽  
Optimum Ph

The study includes partial purification of Lecithin: Cholesterol acyltransferase (LCAT) from the blood serum of a person suffering from atherosclerosis. Several techniques were applied including ammonium sulphate precipitation, dialysis, ion exchange chromatography and electrophoresis. It was found that LCAT has one isoenzyme and the highest activity was (1073.46 × 10-3) unit/ml and a molecular weight of 62 KDa. The study  also deals with characterizing of LCAT. It was found that the optimum pH and temp. of the enzyme were 7 and 35ºC.    http://dx.doi.org/10.25130/tjps.25.2020.027

Separation of oligonucleotides by high-performance ion-exchange chromatography on a non-porous ion exchanger

1988 ◽  
Vol 447 ◽  
pp. 212-220 ◽  
Author(s):  
Yoshio Kato ◽  
Takashi Kitamura ◽  
Akane Mitsui ◽  
Yosuke Yamasaki ◽  
Tsutomu Hashimoto ◽  
...  
Keyword(s):  
Ion Exchange ◽  
High Performance ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Ion Exchanger

Retention model for high-performance ion-exchange chromatography

1983 ◽  
Vol 266 ◽  
pp. 3-21 ◽  
Author(s):  
W. Kopaciewicz ◽  
M.A. Rounds ◽  
J. Fausnaugh ◽  
F.E. Regnier
Keyword(s):  
Ion Exchange ◽  
High Performance ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Retention Model

scholarly journals Isolation of albumin from whole human plasma and fractionation of albumin-depleted plasma

1976 ◽  
Vol 157 (2) ◽  
pp. 301-306 ◽  
Author(s):  
J Travis ◽  
J Bowen ◽  
D Tewksbury ◽  
D Johnson ◽  
R Pannell
Keyword(s):  
Ion Exchange ◽  
Human Plasma ◽  
Plasma Proteins ◽  
Deae Cellulose ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Affinity Column ◽  
Plasma Albumin ◽  
Cibacron Blue ◽  
Blue Sepharose

The dye Cibacron Blue F-3-GA was conjugated to Sepharose to provide an affinity column for serum albumin. Passage of whole human plasma through a column of Cibacron Blue-Sepharose results in the removal of approx. 98% of the albumin. The latter can be quantitatively recovered by desorption with NaSCN. Albumin-depleted plasma can be readily resolved into discrete fractions by a combination of conventional biochemical techniques. In particular, the resolution of plasma proteins with properties similar to those of native human plasma albumin can readily be accomplished by ion-exchange chromatography of the Sepharose-dye-treated plasma on DEAE-cellulose.

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